Header list of 1z31.pdb file
Complete list - 2 20 Bytes
HEADER RNA 10-MAR-05 1Z31
TITLE THE STRUCTURE OF AN ENZYME-ACTIVATING FRAGMENT OF HUMAN TELOMERASE RNA
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: HUMAN TELOMERASE PJ6 HAIRPIN;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: HUMAN TELOMERASE RNA;
COMPND 5 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 SYNTHETIC: YES;
SOURCE 3 OTHER_DETAILS: T7 RNA POLYMERASE IN VITRO TRANSCRIPTION FROM DNA
SOURCE 4 OLIGONUCLEOTIDE TEMPLATE
KEYWDS ASYMMETRIC INTERNAL BULGE, RESIDUAL DIPOLAR COUPLINGS, TELOMERASE
KEYWDS 2 PROTEIN BINDING SITE, RNA
EXPDTA SOLUTION NMR
NUMMDL 10
AUTHOR T.C.LEEPER,G.VARANI
REVDAT 3 02-MAR-22 1Z31 1 REMARK
REVDAT 2 24-FEB-09 1Z31 1 VERSN
REVDAT 1 22-MAR-05 1Z31 0
JRNL AUTH T.C.LEEPER,G.VARANI
JRNL TITL THE STRUCTURE OF AN ENZYME-ACTIVATING FRAGMENT OF HUMAN
JRNL TITL 2 TELOMERASE RNA.
JRNL REF RNA V. 11 394 2005
JRNL REFN ISSN 1355-8382
JRNL PMID 15703438
JRNL DOI 10.1261/RNA.7222505
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : XWINNMR 3.0, X-PLOR 2.9.4
REMARK 3 AUTHORS : BRUNGER AND CLORE (X-PLOR)
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: 726 TOTAL RESTRAINTS, 429 NOE-DERIVED
REMARK 3 RESTRAINTS, 159 DIHEDRAL RESTRAINTS, 65 RESIDUAL DIPOLAR
REMARK 3 COUPLING RESTRAINTS, 62 HYDROGEN BONDS, AND 11 WEAK PLANARITY
REMARK 3 RESTRAINTS.
REMARK 4
REMARK 4 1Z31 COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 11-MAR-05.
REMARK 100 THE DEPOSITION ID IS D_1000032234.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 298; 277
REMARK 210 PH : 6; 6
REMARK 210 IONIC STRENGTH : 10 MM; 10 MM
REMARK 210 PRESSURE : 1 ATM; 1 ATM
REMARK 210 SAMPLE CONTENTS : PJ6 1 MM UNLABELED; 10 MM SODIUM
REMARK 210 PHOSHATE, PH 6.0, 100% D2O; PJ6
REMARK 210 1 MM UNLABELED; 10 MM SODIUM
REMARK 210 PHOSHATE, PH 6.0, 90% H2O, 10%
REMARK 210 D2O; PJ6 0.6 MM U-15N,13C; 10 MM
REMARK 210 SODIUM PHOSHATE, PH 6.0, 100%
REMARK 210 D2O; PJ6 0.6 MM U-15N,13C; 10 MM
REMARK 210 SODIUM PHOSHATE, PH 6.0, 90% H2O,
REMARK 210 10% D2O; PJ6 0.6 MM U-15N,13C;
REMARK 210 10 MM SODIUM SUCCINATE, PH 6.0,
REMARK 210 18 MG/ML PF1 BACTERIAPHAGE, 100%
REMARK 210 D2O
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : 2D TOCSY; 2D NOESY; 3D_13C
REMARK 210 -SEPARATED_NOESY; IPAP-HSQC; HCP
REMARK 210 TRIPLE RESONANCE; 3D 13C-31P
REMARK 210 HETCOR; 3D 13C TOCSY-HSQC; HNN-
REMARK 210 COSY
REMARK 210 SPECTROMETER FIELD STRENGTH : 500 MHZ; 750 MHZ
REMARK 210 SPECTROMETER MODEL : DRX; DMX
REMARK 210 SPECTROMETER MANUFACTURER : BRUKER
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : NMRPIPE 2.3, X-PLOR 2.9.4,
REMARK 210 SPARKY 3.110
REMARK 210 METHOD USED : TORSION ANGLE DYNAMICS
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : 100
REMARK 210 CONFORMERS, NUMBER SUBMITTED : 10
REMARK 210 CONFORMERS, SELECTION CRITERIA : STRUCTURES WITH THE LEAST
REMARK 210 RESTRAINT VIOLATIONS
REMARK 210
REMARK 210 BEST REPRESENTATIVE CONFORMER IN THIS ENSEMBLE : 1
REMARK 210
REMARK 210 REMARK: NULL
REMARK 215
REMARK 215 NMR STUDY
REMARK 215 THE COORDINATES IN THIS ENTRY WERE GENERATED FROM SOLUTION
REMARK 215 NMR DATA. PROTEIN DATA BANK CONVENTIONS REQUIRE THAT
REMARK 215 CRYST1 AND SCALE RECORDS BE INCLUDED, BUT THE VALUES ON
REMARK 215 THESE RECORDS ARE MEANINGLESS.
REMARK 300
REMARK 300 BIOMOLECULE: 1
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON
REMARK 300 BURIED SURFACE AREA.
REMARK 350
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS
REMARK 350 GIVEN BELOW. BOTH NON-CRYSTALLOGRAPHIC AND
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.
REMARK 350
REMARK 350 BIOMOLECULE: 1
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CLOSE CONTACTS
REMARK 500
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.
REMARK 500
REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI DISTANCE
REMARK 500 HO2' A A 289 O5' C A 290 1.35
REMARK 500 H1' C A 262 OP2 G A 263 1.37
REMARK 500 HO2' U A 291 O4' G A 292 1.50
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: COVALENT BOND LENGTHS
REMARK 500
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT: (10X,I3,1X,2(A3,1X,A1,I4,A1,1X,A4,3X),1X,F6.3)
REMARK 500
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996
REMARK 500
REMARK 500 M RES CSSEQI ATM1 RES CSSEQI ATM2 DEVIATION
REMARK 500 1 C A 270 C4' C A 270 C3' -0.088
REMARK 500 2 C A 270 C4' C A 270 C3' -0.087
REMARK 500 3 C A 270 C4' C A 270 C3' -0.087
REMARK 500 4 C A 270 C4' C A 270 C3' -0.087
REMARK 500 5 C A 270 C4' C A 270 C3' -0.087
REMARK 500 7 C A 270 C4' C A 270 C3' -0.087
REMARK 500 8 C A 270 C4' C A 270 C3' -0.089
REMARK 500 9 C A 270 C4' C A 270 C3' -0.086
REMARK 500 10 C A 270 C4' C A 270 C3' -0.088
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: COVALENT BOND ANGLES
REMARK 500
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)
REMARK 500
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996
REMARK 500
REMARK 500 M RES CSSEQI ATM1 ATM2 ATM3
REMARK 500 1 C A 294 C5' - C4' - C3' ANGL. DEV. = -8.6 DEGREES
REMARK 500 2 C A 294 C5' - C4' - C3' ANGL. DEV. = -8.6 DEGREES
REMARK 500 4 C A 294 C5' - C4' - C3' ANGL. DEV. = -8.4 DEGREES
REMARK 500 8 C A 294 C5' - C4' - C3' ANGL. DEV. = -8.5 DEGREES
REMARK 500 9 C A 294 C5' - C4' - C3' ANGL. DEV. = -8.5 DEGREES
REMARK 500 10 U A 272 C5' - C4' - C3' ANGL. DEV. = -8.4 DEGREES
REMARK 500
REMARK 500 REMARK: NULL
DBREF 1Z31 A 257 299 PDB 1Z31 1Z31 257 299
SEQRES 1 A 32 G A G G U C G G C C C G A
SEQRES 2 A 32 C U U C G G U C A C U G C
SEQRES 3 A 32 C A C C U C
CRYST1 1.000 1.000 1.000 90.00 90.00 90.00 P 1 1
ORIGX1 1.000000 0.000000 0.000000 0.00000
ORIGX2 0.000000 1.000000 0.000000 0.00000
ORIGX3 0.000000 0.000000 1.000000 0.00000
SCALE1 1.000000 0.000000 0.000000 0.00000
SCALE2 0.000000 1.000000 0.000000 0.00000
SCALE3 0.000000 0.000000 1.000000 0.00000
MODEL 1
Complete list - 2 20 Bytes